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Difference between revisions of "Glycoside Hydrolase Family 75"
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|'''Clan''' | |'''Clan''' | ||
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|'''Mechanism''' | |'''Mechanism''' | ||
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|'''Active site residues''' | |'''Active site residues''' | ||
| − | | | + | |known |
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|{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | |{{Hl2}} colspan="2" align="center" |'''CAZy DB link''' | ||
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== Substrate specificities == | == Substrate specificities == | ||
| − | Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from | + | Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity <cite>Shimosaka1993 Cheng2000</cite>. The analysis of the final product of hydrolysis of partially ''N''-deacetylated chitosan by the GH75 chitosanase from ''Aspergillus fumigatus'' suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain <cite>Cheng2006</cite>. |
== Kinetics and Mechanism == | == Kinetics and Mechanism == | ||
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== Family Firsts == | == Family Firsts == | ||
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#Cheng2006 pmid=16330537 | #Cheng2006 pmid=16330537 | ||
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</biblio> | </biblio> | ||
Revision as of 12:17, 3 June 2011
This page is currently under construction. This means that the Responsible Curator has deemed that the page's content is not quite up to CAZypedia's standards for full public consumption. All information should be considered to be under revision and may be subject to major changes.
- Author:
- Responsible Curator: ^^^Ryszard Brzezinski^^^
| Glycoside Hydrolase Family GH75 | |
| Clan | Not assigned |
| Mechanism | inverting |
| Active site residues | known |
| CAZy DB link | |
| http://www.cazy.org/GH75.html | |
Substrate specificities
Glycoside hydrolases of family 75 include both eukaryotic (essentially fungal) and prokaryotic proteins. They have so far been characterized only from filamentous fungi. They are primarily of beta-1,4-chitosanases with endo-splitting activity [1, 2]. The analysis of the final product of hydrolysis of partially N-deacetylated chitosan by the GH75 chitosanase from Aspergillus fumigatus suggests that this enzyme cleaves preferentially GlcN-GlcN and GlcNAc-GlcN links in the polysaccharide chain [3].
Kinetics and Mechanism
Family GH46 enzymes utilize an inverting mechanism as shown by NMR [3].
Catalytic Residues
Content is to be added here.
Three-dimensional structures
Content is to be added here.
Family Firsts
- First stereochemistry determination
- Cite some reference here, with a short (1-2 sentence) explanation [4].
- First catalytic nucleophile identification
- Cite some reference here, with a short (1-2 sentence) explanation [5].
- First general acid/base residue identification
- Cite some reference here, with a short (1-2 sentence) explanation [6].
- First 3-D structure
- Cite some reference here, with a short (1-2 sentence) explanation [7].
References
-
Shimosaka M, Nogawa M, Ohno Y, and Okazaki M. Chitosanase from the pathogenic fungus, Fusarium solani f.sp. phaseoli - purification and some properties. Biosci. Biotech. Biochem. 57, 231-235.
- Cheng CY and Li YK. (2000). An Aspergillus chitosanase with potential for large-scale preparation of chitosan oligosaccharides. Biotechnol Appl Biochem. 2000;32(3):197-203. DOI:10.1042/ba20000063 |
- Cheng CY, Chang CH, Wu YJ, and Li YK. (2006). Exploration of glycosyl hydrolase family 75, a chitosanase from Aspergillus fumigatus. J Biol Chem. 2006;281(6):3137-44. DOI:10.1074/jbc.M512506200 |